Characterization of sulfur mustard induced structural modifications in human hemoglobin by liquid chromatography - tandem mass spectrometry
article
In this paper we describe the use of tandem mass spectrometry to identify modified sites in human hemoglobin after in vitro exposure to bis(2- chloroethyl) sulfide (sulfur mustard). Globin isolated from human whole blood which had been exposed to sulfur mustard was degraded with trypsin, and the digests were analyzed by micro LC/MS. Alkylated tryptic fragments (α-T1, α- T4, α-T6, α-T9, β-T1, β-T9, β-T10, β-T11, and β-T10-S-S-β-T12) could be tentatively assigned upon comparison with a digest from nonexposed globin. Subsequent tandem mass spectrometry of these peptides allowed unambiguous assignment of 5 specific modified residues: α-Val-1, α-His-20, β-Val-1, β-His-77, and β-His-97. The results demonstrate the usefulness of microbore LC in combination with tandem mass spectrometry for the structural determination of chemically modified peptides and proteins.
Topics
Liquid chromatographyProtein modificationTandem mass spectrometryAlkylationAmino Acid SequenceCarcinogensChemical Warfare AgentsChromatography, High Pressure LiquidErythrocytesGas ChromatographyMass SpectrometryHemoglobinsMolecular Sequence DataMustard GasPeptide FragmentsSpectrophotometry, UltravioletSulfur RadioisotopesTrypsin
TNO Identifier
233355
ISSN
0893228X
Source
Chemical Research in Toxicology, 9(4), pp. 781-787.
Pages
781-787
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